Evidence map›Paper›PMID 38761213›Full record

ArticleArchives of microbiology2024

A novel type IIb L-asparaginase from Latilactobacillus sakei LK-145: characterization and application.

Shiro Kato, Kazuya Tamura, Yuki Masuda, Morichika Konishi, Kazuya Yamanaka, Tadao Oikawa

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Article in Archives of microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Shiro KatoFaculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki, Kagawa, 761-0795, Japan.
Kazuya TamuraDepartment of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35 Yamate-cho, Suita, Osaka-fu, 564-8680, Japan.
Yuki MasudaDepartment of Microbiological Chemistry, Kobe Pharmaceutical University, 4-9-1 Motoyamakita-machi, Higashinada-ku, Kobe, Hyougo, 658-8558, Japan.
Morichika KonishiDepartment of Microbiological Chemistry, Kobe Pharmaceutical University, 4-9-1 Motoyamakita-machi, Higashinada-ku, Kobe, Hyougo, 658-8558, Japan.
Kazuya YamanakaDepartment of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35 Yamate-cho, Suita, Osaka-fu, 564-8680, Japan.
Tadao OikawaDepartment of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35 Yamate-cho, Suita, Osaka-fu, 564-8680, Japan. oikawa@kansai-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We succeeded in homogeneously expressing and purifying L-asparaginase from Latilactobacillus sakei LK-145 (Ls-Asn1) and its mutated enzymes C196S, C264S, C290S, C196S/C264S, C196S/C290S, C264S/C290S, and C196S/C264S/C290S-Ls-Asn1. Enzymological studies using purified enzymes revealed that all cysteine residues of Ls-Asn1 were found to affect the catalytic activity of Ls-Asn1 to varying degrees. The mutation of Cys196 did not affect the specific activity, but the mutation of Cys264, even a single mutation, significantly decreased the specific activity. Furthermore, C264S/C290S- and C196S/C264S/C290S-Ls-Asn1 almost completely lost their activity, suggesting that C290 cooperates with C264 to influence the catalytic activity of Ls-Asn1. The detailed enzymatic properties of three single-mutated enzymes (C196S, C264S, and C290S-Ls-Asn1) were investigated for comparison with Ls-Asn1. We found that only C196S-Ls-Asn1 has almost the same enzymatic properties as that of Ls-Asn1 except for its increased stability for thermal, pH, and the metals NaCl, KCl, CaCl

Indexed as

AsparaginaseAmino Acid SequenceAntineoplastic AgentsBacillaceaeBacterial ProteinsHumansHydrogen-Ion ConcentrationJurkat CellsKineticsMutationAntineoplastic AgentsAsparaginaseBacterial ProteinsLactic acid bacterial-AsparaginaseLatilactobacillus sakeiLeukemia drugs

Identifiers

PMID38761213

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.